(data stored in SCRATCH zone)

SWISSPROT: D4YXN1_SPHJU

ID   D4YXN1_SPHJU            Unreviewed;       429 AA.
AC   D4YXN1;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 55.
DE   RecName: Full=Histidinol dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729213};
DE            Short=HDH {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099};
DE            EC=1.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729213};
GN   Name=hisD {ECO:0000256|HAMAP-Rule:MF_01024,
GN   ECO:0000313|EMBL:BAI95113.1};
GN   OrderedLocusNames=SJA_C1-02790 {ECO:0000313|EMBL:BAI95113.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95113.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95113.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-
CC       histidinol to L-histidinaldehyde and then to L-histidine.
CC       {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099,
CC       ECO:0000256|SAAS:SAAS00728939}.
CC   -!- CATALYTIC ACTIVITY: L-histidinol + H(2)O + 2 NAD(+) = L-histidine
CC       + 2 NADH. {ECO:0000256|HAMAP-Rule:MF_01024,
CC       ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729200}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-4};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-4};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099,
CC       ECO:0000256|SAAS:SAAS00729141}.
CC   -!- SIMILARITY: Belongs to the histidinol dehydrogenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099,
CC       ECO:0000256|RuleBase:RU004175, ECO:0000256|SAAS:SAAS00827949}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP010803; BAI95113.1; -; Genomic_DNA.
DR   RefSeq; WP_013038912.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-02790; -.
DR   EnsemblBacteria; BAI95113; BAI95113; SJA_C1-02790.
DR   GeneID; 29271982; -.
DR   KEGG; sjp:SJA_C1-02790; -.
DR   eggNOG; ENOG4105CEK; Bacteria.
DR   eggNOG; COG0141; LUCA.
DR   HOGENOM; HOG000243914; -.
DR   KO; K00013; -.
DR   OMA; QAEHDPM; -.
DR   OrthoDB; POG091H03YX; -.
DR   UniPathway; UPA00031; UER00014.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd06572; Histidinol_dh; 1.
DR   HAMAP; MF_01024; HisD; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR001692; Histidinol_DH_CS.
DR   InterPro; IPR022695; Histidinol_DH_monofunct.
DR   InterPro; IPR012131; Hstdl_DH.
DR   Pfam; PF00815; Histidinol_dh; 1.
DR   PIRSF; PIRSF000099; Histidinol_dh; 1.
DR   PRINTS; PR00083; HOLDHDRGNASE.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR00069; hisD; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YXN1.
DR   SWISS-2DPAGE; D4YXN1.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00729217};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00728911};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRSR:PIRSR000099-4, ECO:0000256|SAAS:SAAS00781816};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRNR:PIRNR000099,
KW   ECO:0000256|PIRSR:PIRSR000099-2, ECO:0000256|SAAS:SAAS00751613};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01024,
KW   ECO:0000256|PIRNR:PIRNR000099, ECO:0000256|SAAS:SAAS00751612,
KW   ECO:0000313|EMBL:BAI95113.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01024, ECO:0000256|PIRSR:PIRSR000099-
KW   4, ECO:0000256|SAAS:SAAS00781803}.
FT   ACT_SITE    327    327       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                1}.
FT   ACT_SITE    328    328       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                1}.
FT   METAL       259    259       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   METAL       262    262       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   METAL       361    361       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   METAL       420    420       Zinc. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-4}.
FT   BINDING     130    130       NAD. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-2}.
FT   BINDING     191    191       NAD. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-2}.
FT   BINDING     214    214       NAD. {ECO:0000256|HAMAP-Rule:MF_01024,
FT                                ECO:0000256|PIRSR:PIRSR000099-2}.
FT   BINDING     237    237       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     259    259       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     262    262       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     328    328       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     361    361       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     415    415       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
FT   BINDING     420    420       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01024, ECO:0000256|PIRSR:PIRSR000099-
FT                                3}.
SQ   SEQUENCE   429 AA;  45254 MW;  451088C5877632CD CRC64;
     MTFRLSTTDS DFAAAFAALV DARREADEDV SRDVAAILKR VRAEGDAALA DYTSRFDRHD
     LDVSGWAVEP AQCRKALESI STELRGALEL AAARIAAYHE KQKPQDSDSV DAAGARLGAR
     WSAVDAAGLY VPGGRAAYPS SLLMNVIPAR VAGVRRIAMV TPTPDGEINP LVLAAAAIAG
     IEEIWRVGGA QAVAALAYGT DRIRPVDVIT GPGNAWVAEA KRQLYGVVGI DMVAGPSEIV
     VVADGRNDPD WIAADLLSQS EHDPTSQSIL FTDDAAFADA VAAAVDRRLP LLSTQAVATT
     SWNANGAIIV VRDLDEAMPL VDRLAAEHLE LAVDDPDALF AQVRHAGSVF LGRMTPEAVG
     DYVAGPNHVL PTGRRARFSS GLSVLDFMKR TSFLSLDRRA IDAIGPAAVA LAEAEGLPAH
     AASVALRLK
//

If you have problems or comments...

PBIL Back to PBIL home page